1KVL

X-ray Crystal Structure of AmpC S64G Mutant beta-Lactamase in Complex with Substrate and Product Forms of Cephalothin

Summary for 1KVL

• Entry DOI: 10.2210/pdb1kvl/pdb
• Related: 1KE4 1KVM 2BLS
• Descriptor: Beta-lactamase, PHOSPHATE ION, 2-[CARBOXY-(2-THIOPHEN-2-YL-ACETYLAMINO)-METHYL]-5-METHYL-3,6-DIHYDRO-2H-[1,3]THIAZINE-4-CARBOXYLIC ACID, ... (6 entities in total)
• Functional Keywords: amide hydrolase, beta-lactamase, cephalothin, substrate-enzyme complex, product-enzyme complex, hydrolase
• Biological source: Escherichia coli
• Cellular location: Periplasm: P00811
• Total number of polymer chains: 2
• Total formula weight: 80412.99

Authors

Beadle, B.M.,Trehan, I.,Focia, P.J.,Shoichet, B.K. (deposition date: 2002-01-27, release date: 2002-03-13, Last modification date: 2023-08-16)

• Primary citation: Beadle, B.M.,Trehan, I.,Focia, P.J.,Shoichet, B.K.; Structural milestones in the reaction pathway of an amide hydrolase: substrate, acyl, and product complexes of cephalothin with AmpC beta-lactamase.; Structure, 10:413-424, 2002; PubMed: 12005439; DOI: 10.1016/S0969-2126(02)00725-6

Experimental method

X-RAY DIFFRACTION (1.53 Å)